ArticleBiophysics reports2016
Combining biophysical methods to analyze the disulfide bond in SH2 domain of C-terminal Src kinase.
Article in Biophysics reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Decoding C‑SH2 Domain/Peptide Interactions in SH2 Domain-Containing Tyrosine Phosphatase 2: A Molecular Framework for Rational Inhibitor Design.ACS omega · 2026Article
- Pervanadate-induced oxidation relieves autoinhibition of the protein tyrosine kinase SRC.Science signaling · 2026Article
- Analysis of multi-disulfide bridges for insulin aspart by stepwise reduction and differentiated alkylation.Analytical and bioanalytical chemistry · 2024Article
- Stabilization ofMembranes · 2023Article
- CSK-mediated signalling by integrins in cancer.Frontiers in cell and developmental biology · 2023Review
- Dissection of the catalytic and regulatory structure-function relationships of Csk protein tyrosine kinase.Frontiers in cell and developmental biology · 2023Review
- Cysteines and Disulfide Bonds as Structure-Forming Units: Insights From Different Domains of Life and the Potential for Characterization by NMR.Frontiers in chemistry · 2020Review
- Protein crystal quality oriented disulfide bond engineering.Protein & cell · 2018Article
- Recent mass spectrometry-based techniques and considerations for disulfide bond characterization in proteins.Analytical and bioanalytical chemistry · 2018Review
- Article
- Domain interactions of C-terminal Src Kinase determined through NMR spectroscopy with segmental isotope labeling.Protein & cell · 2017Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
The Src Homology 2 (SH2) domain is a structurally conserved protein domain that typically binds to a phosphorylated tyrosine in a peptide motif from the target protein. The SH2 domain of C-terminal Src kinase (Csk) contains a single disulfide bond, which is unusual for most SH2 domains. Although the global motion of SH2 domain regulates Csk function, little is known about the relationship between the disulfide bond and binding of the ligand. In this study, we combined X-ray crystallography, solution NMR, and other biophysical methods to reveal the interaction network in Csk. Denaturation studies have shown that disulfide bond contributes significantly to the stability of SH2 domain, and crystal structures of the oxidized and C122S mutant showed minor conformational changes. We further investigated the binding of SH2 domain to a phosphorylated peptide from Csk-binding protein upon reduction and oxidation using both NMR and fluorescence approaches. This work employed NMR, X-ray cryptography, and other biophysical methods to study a disulfide bond in Csk SH2 domain. In addition, this work provides in-depth understanding of the structural dynamics of Csk SH2 domain.
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Registered trials
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